(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHN8_GEOS0

ID   A0A0F6BHN8_GEOS0        Unreviewed;       457 AA.
AC   A0A0F6BHN8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 28.
DE   RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555};
GN   Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN   OrderedLocusNames=GY4MC1_0083 {ECO:0000313|EMBL:ADP72939.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72939.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72939.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72939.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase involved in processing of
CC       recombination intermediates, plays a role in repairing DNA breaks.
CC       Stimulates the branch migration of RecA-mediated strand transfer
CC       reactions, allowing the 3' invading strand to extend heteroduplex
CC       DNA faster. Binds ssDNA in the presence of ADP but not other
CC       nucleotides, has ATPase activity that is stimulated by ssDNA and
CC       various branched DNA structures, but inhibited by SSB. Does not
CC       have RecA's homology-searching function.
CC       {ECO:0000256|RuleBase:RU003555}.
CC   -!- FUNCTION: Plays a role in repairing double-strand DNA breaks,
CC       probably involving stabilizing or processing branched DNA or
CC       blocked replication forks. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC   -!- DOMAIN: The middle region has homology to RecA with ATPase motifs
CC       including the RadA KNRFG motif, while the C-terminus is homologous
CC       to Lon protease. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC   -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555}.
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DR   EMBL; CP002293; ADP72939.1; -; Genomic_DNA.
DR   RefSeq; WP_013399823.1; NC_014650.1.
DR   EnsemblBacteria; ADP72939; ADP72939; GY4MC1_0083.
DR   KEGG; gmc:GY4MC1_0083; -.
DR   KO; K04485; -.
DR   OMA; SQVREIT; -.
DR   OrthoDB; 505485at2; -.
DR   BioCyc; GSP581103:G1GOQ-110-MONOMER; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR   CDD; cd01121; Sms; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01498; RadA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004504; DNA_repair_RadA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR041166; Rubredoxin_2.
DR   Pfam; PF18073; Rubredoxin_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00416; sms; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHN8.
DR   SWISS-2DPAGE; A0A0F6BHN8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01498};
KW   Zinc {ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN       69    218       RECA_2. {ECO:0000259|PROSITE:PS50162}.
FT   NP_BIND      98    105       ATP. {ECO:0000256|HAMAP-Rule:MF_01498}.
FT   REGION      354    457       Lon-protease-like. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
FT   MOTIF       255    259       RadA KNRFG motif. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
SQ   SEQUENCE   457 AA;  49821 MW;  A8E9B376F479001F CRC64;
     MGKKKTKFVC QECGYESAKW LGRCPGCNTW NSMVEEIERT KPATKGVFVH SASDIISKPV
     PITTVTATQE PRIQTGISEF NRVLGGGIVK GSLVLIGGDP GIGKSTLLLQ VSAQLAALQH
     KVLYISGEES VKQTKLRADR LHVASDQLYV LAETDLEYIV EAIETIHPVC VVIDSIQTIY
     RADIASAPGS VSQVRECTAE LMKIAKTKGI TIFIVGHVTK EGAIAGPRIL EHMVDTVLYF
     EGERHHTYRI LRAVKNRFGS TNEIGIFEMR ESGLVEVENP SEVFLEERSR GAAGSTVVAA
     MEGTRPVLVE IQALVSPTSF GNPRRMATGI DHNRVSLLMA VLEKRSGLLL QNQDAYLKVA
     GGVKLDEPAI DLAIAVSIAS SFRDQPTNPH DVIIGEVGLT GEVRRVSRIE QRVQEAVKLG
     FSRMIIPKNN LAGWNPPEHI TVIGVSHITE ALEHTLQ
//

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